ID G1XJR2_ARTOA Unreviewed; 641 AA.
AC G1XJR2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=cyclic pyranopterin monophosphate synthase {ECO:0000256|ARBA:ARBA00012575};
DE EC=4.6.1.17 {ECO:0000256|ARBA:ARBA00012575};
GN ORFNames=AOL_s00097g589 {ECO:0000313|EMBL:EGX46685.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX46685.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX46685.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic
CC pyranopterin phosphate + diphosphate; Xref=Rhea:RHEA:49580,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:59648, ChEBI:CHEBI:131766;
CC EC=4.6.1.17; Evidence={ECO:0000256|ARBA:ARBA00001637};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGX46685.1}.
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DR EMBL; ADOT01000177; EGX46685.1; -; Genomic_DNA.
DR RefSeq; XP_011124724.1; XM_011126422.1.
DR AlphaFoldDB; G1XJR2; -.
DR STRING; 756982.G1XJR2; -.
DR GeneID; 22895664; -.
DR eggNOG; KOG2876; Eukaryota.
DR HOGENOM; CLU_009273_7_2_1; -.
DR InParanoid; G1XJR2; -.
DR OMA; YDMCKYA; -.
DR OrthoDB; 9838at2759; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000008784; Unassembled WGS sequence.
DR GO; GO:0019008; C:molybdopterin synthase complex; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0061799; F:cyclic pyranopterin monophosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01420; MoaC_PE; 1.
DR CDD; cd01335; Radical_SAM; 1.
DR CDD; cd21117; Twitch_MoaA; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.30.70.640; Molybdopterin cofactor biosynthesis C (MoaC) domain; 1.
DR HAMAP; MF_01224_B; MoaC_B; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR013483; MoaA.
DR InterPro; IPR010505; MoaA_twitch.
DR InterPro; IPR023045; MoaC.
DR InterPro; IPR047594; MoaC_bact/euk.
DR InterPro; IPR036522; MoaC_sf.
DR InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR02666; moaA; 1.
DR NCBIfam; TIGR00581; moaC; 1.
DR PANTHER; PTHR22960:SF0; MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN 1; 1.
DR PANTHER; PTHR22960; MOLYBDOPTERIN COFACTOR SYNTHESIS PROTEIN A; 1.
DR Pfam; PF01967; MoaC; 1.
DR Pfam; PF06463; Mob_synth_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SUPFAM; SSF55040; Molybdenum cofactor biosynthesis protein C, MoaC; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 87..300
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 641 AA; 70402 MW; E0072F78A6588386 CRC64;
MTTLSTTVRR ALTGQGIHIQ ATLPRPTSYT AVYKISRRNI TSDAATAPVY TQNTERSFQD
DVFAPPTRPS LPATEFSDRM AAIREAKPFS EFLTDNFNRQ HNYLRLYCMP EEGIDLSPPS
HLLTTEEILH LAKLFVSQGV TKIRLTGGEP TVRKDIVDLI TELGKLKAMG LKELAMTTNG
ISLARKLPQM VAGGLTALNL SLDTLDEFKF QFMTRRKGLS NVLKSIDAAL SLNIQPLKVN
CVVMSKVNVD EIPSFLAMTK DKPIEVRFIE YMPFTGNKWE SGKMITYQEM LDQIRQSHPD
LQKVQDHKND TSKTYQIPGY KGKLGFITSM THNFCGTCNR LRITSDGNIK VCLFDNAEVS
LRDMMRKEGG MGPEGEKRLL EVIGVAVKGK KEKHAGLDGV NMLWGCGSLS SGQWLIRAAG
NGSRRPLSKT ISDIPTYLLS PPAPHICQIV RAYSTSRIHR QPTMGTDSQD PAPGQKLTHV
LPSGAAHMVP IHEKAITTRT AKAVSTIKFS NPDAVRLIRS NSNKKGDVLS ISRIAGIMAA
KKTSEIIPLC HPISISKVQV NLRVVDDGNG AIEILTVVTC DGKTGVEMEA LTAATGAALT
VYDMCKAVDK GMVLDGTRVV EKVGGKSGDW KEEGWVEWSE S
//
